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Ultimate Fate (ultimate + fate)
Selected AbstractsAcceleration of nitric oxide autoxidation and nitrosation by membranesIUBMB LIFE, Issue 4-5 2007Matias N. Möller Abstract The reaction between nitric oxide (,NO) and oxygen yields reactive species capable of oxidizing and nitrosating proteins, as well as deaminating DNA bases. Although this reaction is considered too slow to be biologically relevant, it has been shown that membranes, lipoproteins, mitochondria and possibly proteins can accelerate this reaction. This effect stems from the higher solubility of both ,NO and O2in the hydrophobic phase of these biological particles, leading to a concentration of both reagents and so a higher rate of reaction. It has been determined that this reaction occurs from 30 to 300 times more rapidly within the membrane, while even higher values have been suggested for proteins. The autoxidation of ,NO in membranes is not the main route for cellular ,NO consumption but an important consequence of this phenomenon is to focus the generation of significant amounts of oxidizing and nitrosating molecules (nitrogen dioxide and dinitrogen trioxide) in the small volume comprised by cellular membranes. Even so, these reactive species are diffusible and their ultimate fate will depend on the reactivity towards available substrates rather than on physical barriers. The acceleration of ,NO autoxidation by biological hydrophobic phases may thus be a general phenomenon that increases in importance in cases of ,NO overproduction. IUBMB Life, 59: 243-248, 2007 [source] Quantitative analysis of agonist-dependent parathyroid hormone receptor trafficking in whole cells using a functional green fluorescent protein conjugateJOURNAL OF CELLULAR PHYSIOLOGY, Issue 3 2001Bruce R. Conway Many G-protein coupled receptors (GPCRs) undergo ligand-dependent internalization upon activation. The parathyroid hormone (PTH) receptor undergoes endocytosis following prolonged exposure to ligand although the ultimate fate of the receptor following internalization is largely unknown. To investigate compartmentalization of the PTH receptor, we have established a stable cell line expressing a PTH receptor,green fluorescent protein (PTHR,GFP) conjugate and an algorithm to quantify PTH receptor internalization. HEK 293 cells expressing the PTHR,GFP were compared with cells expressing the wild-type PTH receptor in whole-cell binding and functional assays. 125I-PTH binding studies revealed similar Bmax and kD values in cells expressing either the PTHR,GFP or the wild-type PTH receptor. PTH-induced cAMP accumulation was similar in both cell lines suggesting that addition of the GFP to the cytoplasmic tail of the PTH receptor does not alter the ligand binding or G-protein coupling properties of the receptor. Using confocal fluorescence microscopy, we demonstrated that PTH treatment of cells expressing the PTHR,GFP conjugate produced a time-dependent redistribution of the receptor to the endosomal compartment which was blocked by pretreatment with PTH antagonist peptides. Treatment with hypertonic sucrose prevented PTH-induced receptor internalization, suggesting that the PTH receptor internalizes via a clathrin-dependent mechanism. Moreover, co-localization with internalized transferrin showed that PTHR,GFP trafficking utilized the endocytic recycling compartment. Experiments using cycloheximide to inhibit protein synthesis demonstrated that recycling of the PTHR,GFP back to the plasma membrane was complete within 1,2 h of ligand removal and was partially blocked by pretreatment with cytochalasin D, but not nocodazole. We also demonstrated that the PTH receptor, upon recycling to the plasma membrane, is capable of undergoing a second round of internalization, a finding consistent with a role for receptor recycling in functional resensitization. © 2001 Wiley-Liss, Inc. [source] The life and death of planet Earth: How the new science of astrobiology charts the ultimate fate of our world.METEORITICS & PLANETARY SCIENCE, Issue 7 2003Donald Brownlee, Peter D. Ward [source] Root dynamics and global change: seeking an ecosystem perspectiveNEW PHYTOLOGIST, Issue 1 2000RICHARD J. NORBY Changes in the production and turnover of roots in forests and grasslands in response to rising atmospheric CO2 concentrations, elevated temperatures, altered precipitation, or nitrogen deposition could be a key link between plant responses and longer-term changes in soil organic matter and ecosystem carbon balance. Here we summarize the experimental observations, ideas, and new hypotheses developed in this area in the rest of this volume. Three central questions are posed. Do elevated atmospheric CO2, nitrogen deposition, and climatic change alter the dynamics of root production and mortality? What are the consequences of root responses to plant physiological processes? What are the implications of root dynamics to soil microbial communities and the fate of carbon in soil? Ecosystem-level observations of root production and mortality in response to global change parameters are just starting to emerge. The challenge to root biologists is to overcome the profound methodological and analytical problems and assemble a more comprehensive data set with sufficient ancillary data that differences between ecosystems can be explained. The assemblage of information reported herein on global patterns of root turnover, basic root biology that controls responses to environmental variables, and new observations of root and associated microbial responses to atmospheric and climatic change helps to sharpen our questions and stimulate new research approaches. New hypotheses have been developed to explain why responses of root turnover might differ in contrasting systems, how carbon allocation to roots is controlled, and how species differences in root chemistry might explain the ultimate fate of carbon in soil. These hypotheses and the enthusiasm for pursuing them are based on the firm belief that a deeper understanding of root dynamics is critical to describing the integrated response of ecosystems to global change. [source] |